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Literature summary for 4.1.3.4 extracted from

  • Forouhar, F.; Hussain, M.; Farid, R.; Benach, J.; Abashidze, M.; Edstrom, W.C.; Vorobiev, S.M.; Xiao, R.; Acton, T.B.; Fu, Z.; Kim, J.J.; Miziorko, H.M.; Montelione, G.T.; Hunt, J.F.
    Crystal structures of two bacterial Hmg-CoA lyases suggest a common catalytic mechanism among a family of TIM-barrel metalloenzymes cleaving carbon-carbon bonds (2005), J. Biol. Chem., 281, 7533-7545.
    View publication on PubMed
Search for more literature for 4.1.3.4

Application

Application Comment Organism
medicine mutations in this enzyme cause a human autosomal recessive disorder called primary metabolic aciduria Bacillus subtilis
medicine mutations in this enzyme cause a human autosomal recessive disorder called primary metabolic aciduria Brucella melitensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis
expression in Escherichia coli Brucella melitensis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method with 19% (w/v) PEG 3350, 200 mM CaCl2, 10 mM dithiothreitol Brucella melitensis
hanging drop vapour diffusion method with 22.5% (w/v) PEG 3350, 210 mM sodium iodide, 5 mM EDTA, 10 mM dithiothreitol Bacillus subtilis
hanging-drop vapour diffusion method Bacillus subtilis
hanging-drop vapour diffusion method Brucella melitensis

Protein Variants

Protein Variants Comment Organism
A252A decreased Km relative to the wild type enzyme Brucella melitensis
C238A increased Km relative to the wild type enzyme Brucella melitensis
C238S decreased Km relative to the wild type enzyme Brucella melitensis
C240A increased Km relative to the wild type enzyme Bacillus subtilis
C240S decreased Km relative to the wild type enzyme Bacillus subtilis
D14E decreased Km relative to the wild type enzyme Brucella melitensis
D16E decreased Km relative to the wild type enzyme Bacillus subtilis
D16N decreased Km relative to the wild type enzyme Bacillus subtilis
D176A increased Km relative to the wild type enzyme Brucella melitensis
D178A increased Km relative to the wild type enzyme Bacillus subtilis
D254A decreased Km relative to the wild type enzyme Bacillus subtilis
E11D decreased Km relative to the wild type enzyme Bacillus subtilis
E253A decreased Km relative to the wild type enzyme Bacillus subtilis
E44A increased Km relative to the wild type enzyme Brucella melitensis
E46A increased Km relative to the wild type enzyme Bacillus subtilis
E9D decreased Km relative to the wild type enzyme Brucella melitensis
H205A increased Km relative to the wild type enzyme Brucella melitensis
H205D increased Km relative to the wild type enzyme Brucella melitensis
H205R decreased Km relative to the wild type enzyme Brucella melitensis
H207A increased Km relative to the wild type enzyme Bacillus subtilis
H207D increased Km relative to the wild type enzyme Bacillus subtilis
H207R decreased Km relative to the wild type enzyme Bacillus subtilis
K297S increased Km relative to the wild type enzyme Bacillus subtilis
R13Q increased Km relative to the wild type enzyme Brucella melitensis
R15Q increased Km relative to the wild type enzyme Bacillus subtilis
V251A decreased Km relative to the wild type enzyme Brucella melitensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ can replace Mn2+ required for activity Bacillus subtilis
Mg2+ can replace Mn2+ required for activity Brucella melitensis
Mn2+ required for activity Bacillus subtilis
Mn2+ required for activity Brucella melitensis
additional information reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg Bacillus subtilis
additional information reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg Brucella melitensis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34873
-
-
Brucella melitensis Q8YEF2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis
-
 Brucella melitensis
nickel-nitrilotriacetic acid column chromatography and Superdex 75 gel filtration Bacillus subtilis
nickel-nitrilotriacetic acid column chromatography and Superdex 75 gel filtration Brucella melitensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-3-Hydroxy-3-methylglutaryl-CoA
-
 Bacillus subtilis Acetyl-CoA + acetoacetate
-
 ?
(S)-3-Hydroxy-3-methylglutaryl-CoA
-
 Brucella melitensis Acetyl-CoA + acetoacetate
-
 ?

Subunits

Subunits Comment Organism
dimer static light scattering, crystal contains two dimers forming a pseudotetramer per asymmetric unit Bacillus subtilis
dimer static light scattering, crystal contains two dimers forming a pseudotetramer per asymmetric unit Brucella melitensis

Synonyms

Synonyms Comment Organism
3-hydroxy-3-methylglutarate-CoA lyase
-
 Bacillus subtilis
3-hydroxy-3-methylglutarate-CoA lyase
-
 Brucella melitensis
HMG-CoA lyase
-
 Bacillus subtilis
HMG-CoA lyase
-
 Brucella melitensis
HMG-CoA lyase belongs to the family of DRE-TIM metallolyases Bacillus subtilis
HMG-CoA lyase belongs to the family of DRE-TIM metallolyases Brucella melitensis